Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction
Само за регистроване кориснике
2022
Конференцијски прилог (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The main goal of this work was the elucidation of the binding interactions between bovine serum
albumin (BSA) and methionine coated silver nanoparticles (AgNPs) under physiological like
conditions using fluorescence spectroscopy techniques. The quenching of BSA’s tryptophan
fluorescence has occurred at the concentration-dependent manner. The linear shape obtained for
Stern-Volmer plots and its larger slope at higher temperatures indicated mixed static and dynamic
quenching mechanisms. The values of quenching constants, Ksv and the bimolecular quenching rate
constants, kq, pointed out the existence of binding interactions between BSA and AgNPs. The
binding constants, K, with values around 1 × 104
M-1, indicated low to moderate binding interaction
with one binding site. Determined thermodynamic parameters ΔHo < 0, ΔSo < 0 and ΔGo
< 0 at different temperatures pointed out spontaneous processes, where hydrogen and van der Waals
interactions play a major role in the binding.
Извор:
PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings, 2022, 2, 609-612Издавач:
- Belgrade : Society of Physical Chemists of Serbia
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200017 (Универзитет у Београду, Институт за нуклеарне науке Винча, Београд-Винча) (RS-MESTD-inst-2020-200017)
Напомена:
- XVI International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings. Vol. 2, September 26-30, Belgrade.
Колекције
Институција/група
VinčaTY - CONF AU - Bondžić, Aleksandra AU - Jovanović, Dunja PY - 2022 UR - https://vinar.vin.bg.ac.rs/handle/123456789/12681 AB - The main goal of this work was the elucidation of the binding interactions between bovine serum albumin (BSA) and methionine coated silver nanoparticles (AgNPs) under physiological like conditions using fluorescence spectroscopy techniques. The quenching of BSA’s tryptophan fluorescence has occurred at the concentration-dependent manner. The linear shape obtained for Stern-Volmer plots and its larger slope at higher temperatures indicated mixed static and dynamic quenching mechanisms. The values of quenching constants, Ksv and the bimolecular quenching rate constants, kq, pointed out the existence of binding interactions between BSA and AgNPs. The binding constants, K, with values around 1 × 104 M-1, indicated low to moderate binding interaction with one binding site. Determined thermodynamic parameters ΔHo < 0, ΔSo < 0 and ΔGo < 0 at different temperatures pointed out spontaneous processes, where hydrogen and van der Waals interactions play a major role in the binding. PB - Belgrade : Society of Physical Chemists of Serbia C3 - PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings T1 - Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction VL - 2 SP - 609 EP - 612 UR - https://hdl.handle.net/21.15107/rcub_vinar_12681 ER -
@conference{ author = "Bondžić, Aleksandra and Jovanović, Dunja", year = "2022", abstract = "The main goal of this work was the elucidation of the binding interactions between bovine serum albumin (BSA) and methionine coated silver nanoparticles (AgNPs) under physiological like conditions using fluorescence spectroscopy techniques. The quenching of BSA’s tryptophan fluorescence has occurred at the concentration-dependent manner. The linear shape obtained for Stern-Volmer plots and its larger slope at higher temperatures indicated mixed static and dynamic quenching mechanisms. The values of quenching constants, Ksv and the bimolecular quenching rate constants, kq, pointed out the existence of binding interactions between BSA and AgNPs. The binding constants, K, with values around 1 × 104 M-1, indicated low to moderate binding interaction with one binding site. Determined thermodynamic parameters ΔHo < 0, ΔSo < 0 and ΔGo < 0 at different temperatures pointed out spontaneous processes, where hydrogen and van der Waals interactions play a major role in the binding.", publisher = "Belgrade : Society of Physical Chemists of Serbia", journal = "PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings", title = "Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction", volume = "2", pages = "609-612", url = "https://hdl.handle.net/21.15107/rcub_vinar_12681" }
Bondžić, A.,& Jovanović, D.. (2022). Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction. in PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings Belgrade : Society of Physical Chemists of Serbia., 2, 609-612. https://hdl.handle.net/21.15107/rcub_vinar_12681
Bondžić A, Jovanović D. Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction. in PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings. 2022;2:609-612. https://hdl.handle.net/21.15107/rcub_vinar_12681 .
Bondžić, Aleksandra, Jovanović, Dunja, "Quenching of bovine serum albumin fluorescence by methionine coated silver nanoparticles: Insight in the mechanism of interaction" in PHYSICAL CHEMISTRY 2022 : 16th International Conference on Fundamental and Applied Aspects of Physical Chemistry : Proceedings, 2 (2022):609-612, https://hdl.handle.net/21.15107/rcub_vinar_12681 .